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The Bor1 elevator transport cycle is subject to autoinhibition and activation

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  • Yan Jiang

    (National Institutes of Health
    University of Sydney)

  • Jiansen Jiang

    (National Institutes of Health)

Abstract

Boron, essential for plant growth, necessitates precise regulation due to its potential toxicity. This regulation is achieved by borate transporters (BORs), which are homologous to the SLC4 family. The Arabidopsis thaliana Bor1 (AtBor1) transporter from clade I undergoes slow regulation through degradation and translational suppression, but its potential for fast regulation via direct activity modulation was unclear. Here, we combine cryo-electron microscopy, mutagenesis, and functional characterization to study AtBor1, revealing high-resolution structures of the dimer in one inactive and three active states. Our findings show that AtBor1 is regulated by two distinct mechanisms: an autoinhibitory domain at the carboxyl terminus obstructs the substrate pathway via conserved salt bridges, and phosphorylation of Thr410 allows interaction with a positively charged pocket at the cytosolic face, essential for borate transport. These results elucidate the molecular basis of AtBor1’s activity regulation and highlight its role in fast boron level regulation in plants.

Suggested Citation

  • Yan Jiang & Jiansen Jiang, 2024. "The Bor1 elevator transport cycle is subject to autoinhibition and activation," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53411-1
    DOI: 10.1038/s41467-024-53411-1
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    1. Qing Zhang & Liyan Jian & Deqiang Yao & Bing Rao & Ying Xia & Kexin Hu & Shaobai Li & Yafeng Shen & Mi Cao & An Qin & Jie Zhao & Yu Cao, 2023. "The structural basis of the pH-homeostasis mediated by the Cl−/HCO3− exchanger, AE2," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Feiran Lu & Shuo Li & Yang Jiang & Jing Jiang & He Fan & Guifeng Lu & Dong Deng & Shangyu Dang & Xu Zhang & Jiawei Wang & Nieng Yan, 2011. "Structure and mechanism of the uracil transporter UraA," Nature, Nature, vol. 472(7342), pages 243-246, April.
    3. Junpei Takano & Kyotaro Noguchi & Miho Yasumori & Masaharu Kobayashi & Zofia Gajdos & Kyoko Miwa & Hiroaki Hayashi & Tadakatsu Yoneyama & Toru Fujiwara, 2002. "Arabidopsis boron transporter for xylem loading," Nature, Nature, vol. 420(6913), pages 337-340, November.
    4. Kevin W. Huynh & Jiansen Jiang & Natalia Abuladze & Kirill Tsirulnikov & Liyo Kao & Xuesi Shao & Debra Newman & Rustam Azimov & Alexander Pushkin & Z. Hong Zhou & Ira Kurtz, 2018. "CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    5. Yishuo Lu & Peng Zuo & Hongyi Chen & Hui Shan & Weize Wang & Zonglin Dai & He Xu & Yayu Chen & Ling Liang & Dian Ding & Yan Jin & Yuxin Yin, 2023. "Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIP2," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    6. Weiguang Wang & Kirill Tsirulnikov & Hristina R. Zhekova & Gülru Kayık & Hanif Muhammad Khan & Rustam Azimov & Natalia Abuladze & Liyo Kao & Debbie Newman & Sergei Yu. Noskov & Z. Hong Zhou & Alexande, 2021. "Cryo-EM structure of the sodium-driven chloride/bicarbonate exchanger NDCBE," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
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